|
Name |
Accession |
Description |
Interval |
E-value |
| GlxA |
COG4977 |
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ... |
180-284 |
1.57e-24 |
|
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH domain [Transcription];
Pssm-ID: 444002 [Multi-domain] Cd Length: 318 Bit Score: 100.23 E-value: 1.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654551502 180 RIMSWIEAHYASKFSLDQLAHDLGLSRSYTSRIFRQQTGGSIHEYLLTRRIKSSCDLLRYSDESIDTIALAVGFSEVTYF 259
Cdd:COG4977 214 RAQAWMEANLEEPLSVDELARRAGMSPRTLERRFRAATGTTPARYLQRLRLERARRLLETTDLSIEEIAAACGFGSASHF 293
|
90 100
....*....|....*....|....*
gi 654551502 260 ITCFKKMMRQTPLQYRRRILSTRMP 284
Cdd:COG4977 294 RRAFRRRFGVSPSAYRRRFRARAAA 318
|
|
| HTH_ARAC |
smart00342 |
helix_turn_helix, arabinose operon control protein; |
192-275 |
3.68e-22 |
|
helix_turn_helix, arabinose operon control protein;
Pssm-ID: 197666 [Multi-domain] Cd Length: 84 Bit Score: 87.61 E-value: 3.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654551502 192 KFSLDQLAHDLGLSRSYTSRIFRQQTGGSIHEYLLTRRIKSSCDLLRYSDESIDTIALAVGFSEVTYFITCFKKMMRQTP 271
Cdd:smart00342 1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80
|
....
gi 654551502 272 LQYR 275
Cdd:smart00342 81 SEYR 84
|
|
| AraC |
COG2207 |
AraC-type DNA-binding domain and AraC-containing proteins [Transcription]; |
17-280 |
1.14e-21 |
|
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
Pssm-ID: 441809 [Multi-domain] Cd Length: 258 Bit Score: 91.38 E-value: 1.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654551502 17 ISFNRLYASSAIYYHWHQCVELLYISSGYGIVVVDNQHYTARPGRLFIFPPFRLHKVQVDHSDKNPYHRTTMHIEQAVVE 96
Cdd:COG2207 1 LRLLILLLLLLLLLALLLLLLLLLLLLILLLLALVLLLLLLALLLLLLLLLGLLGGLLLLLLLLLLLGLLLLLLLLLLGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654551502 97 SALSAFPRHQARFAALAASNLPAQIYDLSEHAAFIERILEQFQRLEGNEQTEACEVAFLVMQLMTFLPEQPQPYPPRQQT 176
Cdd:COG2207 81 LLLALLALLLLVGLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLRALELLLLLLLLLLLLLLLLLLLLLLLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654551502 177 VASRIMSWIeahyaskfSLDQLAHDLGLSRSYTSRIFRQQTGGSIHEYLLTRRIKSSCDLLRYSDESIDTIALAVGFSEV 256
Cdd:COG2207 161 LLLLLLLLL--------TLEELARELGLSPRTLSRLFKEETGTSPKQYLRELRLERAKRLLAETDLSISEIAYELGFSSQ 232
|
250 260
....*....|....*....|....
gi 654551502 257 TYFITCFKKMMRQTPLQYRRRILS 280
Cdd:COG2207 233 SHFSRAFKKRFGVTPSEYRKRLRA 256
|
|
| HTH_18 |
pfam12833 |
Helix-turn-helix domain; |
198-277 |
1.06e-18 |
|
Helix-turn-helix domain;
Pssm-ID: 432818 [Multi-domain] Cd Length: 81 Bit Score: 78.40 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654551502 198 LAHDLGLSRSYTSRIFRQQTGGSIHEYLLTRRIKSSCDLL-RYSDESIDTIALAVGFSEVTYFITCFKKMMRQTPLQYRR 276
Cdd:pfam12833 1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLlEDTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYRR 80
|
.
gi 654551502 277 R 277
Cdd:pfam12833 81 R 81
|
|
| PRK10572 |
PRK10572 |
arabinose operon transcriptional regulator AraC; |
44-278 |
2.98e-13 |
|
arabinose operon transcriptional regulator AraC;
Pssm-ID: 236717 [Multi-domain] Cd Length: 290 Bit Score: 68.46 E-value: 2.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654551502 44 GYGIVVVDNQHYTARPGRLFIFPPFRLHKVQVDHSDKNPYHRTTMHIeqavvesalsafPRhqARFAA-LAASNLPAQIY 122
Cdd:PRK10572 58 GQGVIFNGGRAFVCRPGDLLLFPPGEIHHYGRHPDSDEWYHQWVYFR------------PR--AYWADwLNWPSIFAGVG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654551502 123 DLSEHAafiERILEQFQRLEGN-EQTEACEVAF---LVMQLMT--FLPEQPQPYPPRQQTVASRI---MSWIEAHYASKF 193
Cdd:PRK10572 124 RLRIPD---EALQPEFSDLFGQiEQAGQSEGRYselLAMNLLErlLLRCMEAIPESLHPPMDPRVreaCQYISDHLASEF 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654551502 194 SLDQLAHDLGLSRSYTSRIFRQQTGGSIHEYLLTRRIKSSCDLLRYSDESIDTIALAVGFSEVTYFITCFKKMMRQTPLQ 273
Cdd:PRK10572 201 DIESVAQHVCLSPSRLAHLFRQQLGISVLRWREDQRISRAKLLLQTTRMPIATIGRNVGYDDQLYFSRVFKKCTGASPSE 280
|
....*
gi 654551502 274 YRRRI 278
Cdd:PRK10572 281 FRARC 285
|
|
| PRK13503 |
PRK13503 |
HTH-type transcriptional activator RhaS; |
131-275 |
9.84e-13 |
|
HTH-type transcriptional activator RhaS;
Pssm-ID: 184094 [Multi-domain] Cd Length: 278 Bit Score: 66.62 E-value: 9.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654551502 131 IERILEQFQRLEGNEQTEA-CEVAFLVMQLMTFLPEQPQPYPPRQQTVASR-IMSWIEAHYASKFSLDQLAHDLGLSRSY 208
Cdd:PRK13503 124 VRQLVAQMEQQEESNDLEAiASREILFMQLLVLLRKSSLQENGENSDARLNqLLAWLEDHFAEEVNWEALADQFSLSLRT 203
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 654551502 209 TSRIFRQQTGGSIHEYLLTRRIKSSCDLLRYSDESIDTIALAVGFSEVTYFITCFKKMMRQTPLQYR 275
Cdd:PRK13503 204 LHRQLKQQTGLTPQRYLNRLRLLKARHLLRHSDASVTDIAYRCGFGDSNHFSTLFRREFSWSPRDIR 270
|
|
| AraC_binding |
pfam02311 |
AraC-like ligand binding domain; This family represents the arabinose-binding and dimerization ... |
30-137 |
4.13e-07 |
|
AraC-like ligand binding domain; This family represents the arabinose-binding and dimerization domain of the bacterial gene regulatory protein AraC. The domain is found in conjunction with the helix-turn-helix (HTH) DNA-binding motif pfam00165. This domain is distantly related to the Cupin domain pfam00190.
Pssm-ID: 396749 [Multi-domain] Cd Length: 134 Bit Score: 48.20 E-value: 4.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654551502 30 YHWHQCVELLYISSGYGIVVVDNQHYTARPGRLFIFPPFRLHKVQVDHSDknPYHRTTMHIEQAVVESALSAFPRHQARF 109
Cdd:pfam02311 18 PHVHDFYVIGYIERGVGRFRLNGRTYHLGPGDLFLLPPGEPHDYEPESED--GWRYRWLYFEPELLERILADISILAGGP 95
|
90 100 110
....*....|....*....|....*....|..
gi 654551502 110 AAL----AASNLPAQIYDLSEHAAFIERILEQ 137
Cdd:pfam02311 96 LPLlrdpELAALLRALFRLLEEAGRSDDLLAE 127
|
|
| cupin_MmsR-like_N |
cd06986 |
AraC/XylS family transcriptional regulators similar to MmsR, N-terminal cupin domain; This ... |
38-79 |
2.81e-05 |
|
AraC/XylS family transcriptional regulators similar to MmsR, N-terminal cupin domain; This family contains bacterial proteins containing an AraC/XylS family helix-turn-helix (HTH) DNA-binding domain C-terminal to a cupin domain, and may be possible transcriptional regulators. Included is MmsR, a bacterial transcriptional regulator thought to positively regulate the expression of the mmsAB operon. The mmsAB operon contains two structural genes involved in valine metabolism: mmsA which encodes methylmalonate-semialdehyde dehydrogenase, and mmsB which encodes 3-hydroxyisobutyrate dehydrogenase. The cupin domain of members of this subfamily does not contain a metal binding site.
Pssm-ID: 380391 [Multi-domain] Cd Length: 84 Bit Score: 41.70 E-value: 2.81e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 654551502 38 LLYISSGYGIVVVDNQHYTARPGRLFIFPPFRLHKVQVDHSD 79
Cdd:cd06986 31 LHYVLSGKGTFSVNGKTYHLKAGQGFLIPPGEPHSYGADEDD 72
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GlxA |
COG4977 |
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ... |
180-284 |
1.57e-24 |
|
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH domain [Transcription];
Pssm-ID: 444002 [Multi-domain] Cd Length: 318 Bit Score: 100.23 E-value: 1.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654551502 180 RIMSWIEAHYASKFSLDQLAHDLGLSRSYTSRIFRQQTGGSIHEYLLTRRIKSSCDLLRYSDESIDTIALAVGFSEVTYF 259
Cdd:COG4977 214 RAQAWMEANLEEPLSVDELARRAGMSPRTLERRFRAATGTTPARYLQRLRLERARRLLETTDLSIEEIAAACGFGSASHF 293
|
90 100
....*....|....*....|....*
gi 654551502 260 ITCFKKMMRQTPLQYRRRILSTRMP 284
Cdd:COG4977 294 RRAFRRRFGVSPSAYRRRFRARAAA 318
|
|
| AdaA |
COG2169 |
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ... |
176-277 |
2.81e-22 |
|
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), contains Zn-binding and two AraC-type DNA-binding domains [Replication, recombination and repair];
Pssm-ID: 441772 [Multi-domain] Cd Length: 358 Bit Score: 94.74 E-value: 2.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654551502 176 TVASRIMSWIEAHYASKFSLDQLAHDLGLSRSYTSRIFRQQTGGSIHEYLLTRRIKSSCDLLRySDESIDTIALAVGFSE 255
Cdd:COG2169 84 DLVARACRLIEAGAEDRPSLEDLAARLGLSPRHLRRLFKAHTGVTPKAYARARRLLRARQLLQ-TGLSVTDAAYAAGFGS 162
|
90 100
....*....|....*....|..
gi 654551502 256 VTYFITCFKKMMRQTPLQYRRR 277
Cdd:COG2169 163 LSRFYEAFKKLLGMTPSAYRRG 184
|
|
| HTH_ARAC |
smart00342 |
helix_turn_helix, arabinose operon control protein; |
192-275 |
3.68e-22 |
|
helix_turn_helix, arabinose operon control protein;
Pssm-ID: 197666 [Multi-domain] Cd Length: 84 Bit Score: 87.61 E-value: 3.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654551502 192 KFSLDQLAHDLGLSRSYTSRIFRQQTGGSIHEYLLTRRIKSSCDLLRYSDESIDTIALAVGFSEVTYFITCFKKMMRQTP 271
Cdd:smart00342 1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80
|
....
gi 654551502 272 LQYR 275
Cdd:smart00342 81 SEYR 84
|
|
| AraC |
COG2207 |
AraC-type DNA-binding domain and AraC-containing proteins [Transcription]; |
17-280 |
1.14e-21 |
|
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
Pssm-ID: 441809 [Multi-domain] Cd Length: 258 Bit Score: 91.38 E-value: 1.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654551502 17 ISFNRLYASSAIYYHWHQCVELLYISSGYGIVVVDNQHYTARPGRLFIFPPFRLHKVQVDHSDKNPYHRTTMHIEQAVVE 96
Cdd:COG2207 1 LRLLILLLLLLLLLALLLLLLLLLLLLILLLLALVLLLLLLALLLLLLLLLGLLGGLLLLLLLLLLLGLLLLLLLLLLGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654551502 97 SALSAFPRHQARFAALAASNLPAQIYDLSEHAAFIERILEQFQRLEGNEQTEACEVAFLVMQLMTFLPEQPQPYPPRQQT 176
Cdd:COG2207 81 LLLALLALLLLVGLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLRALELLLLLLLLLLLLLLLLLLLLLLLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654551502 177 VASRIMSWIeahyaskfSLDQLAHDLGLSRSYTSRIFRQQTGGSIHEYLLTRRIKSSCDLLRYSDESIDTIALAVGFSEV 256
Cdd:COG2207 161 LLLLLLLLL--------TLEELARELGLSPRTLSRLFKEETGTSPKQYLRELRLERAKRLLAETDLSISEIAYELGFSSQ 232
|
250 260
....*....|....*....|....
gi 654551502 257 TYFITCFKKMMRQTPLQYRRRILS 280
Cdd:COG2207 233 SHFSRAFKKRFGVTPSEYRKRLRA 256
|
|
| HTH_18 |
pfam12833 |
Helix-turn-helix domain; |
198-277 |
1.06e-18 |
|
Helix-turn-helix domain;
Pssm-ID: 432818 [Multi-domain] Cd Length: 81 Bit Score: 78.40 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654551502 198 LAHDLGLSRSYTSRIFRQQTGGSIHEYLLTRRIKSSCDLL-RYSDESIDTIALAVGFSEVTYFITCFKKMMRQTPLQYRR 276
Cdd:pfam12833 1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLlEDTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYRR 80
|
.
gi 654551502 277 R 277
Cdd:pfam12833 81 R 81
|
|
| PRK10572 |
PRK10572 |
arabinose operon transcriptional regulator AraC; |
44-278 |
2.98e-13 |
|
arabinose operon transcriptional regulator AraC;
Pssm-ID: 236717 [Multi-domain] Cd Length: 290 Bit Score: 68.46 E-value: 2.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654551502 44 GYGIVVVDNQHYTARPGRLFIFPPFRLHKVQVDHSDKNPYHRTTMHIeqavvesalsafPRhqARFAA-LAASNLPAQIY 122
Cdd:PRK10572 58 GQGVIFNGGRAFVCRPGDLLLFPPGEIHHYGRHPDSDEWYHQWVYFR------------PR--AYWADwLNWPSIFAGVG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654551502 123 DLSEHAafiERILEQFQRLEGN-EQTEACEVAF---LVMQLMT--FLPEQPQPYPPRQQTVASRI---MSWIEAHYASKF 193
Cdd:PRK10572 124 RLRIPD---EALQPEFSDLFGQiEQAGQSEGRYselLAMNLLErlLLRCMEAIPESLHPPMDPRVreaCQYISDHLASEF 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654551502 194 SLDQLAHDLGLSRSYTSRIFRQQTGGSIHEYLLTRRIKSSCDLLRYSDESIDTIALAVGFSEVTYFITCFKKMMRQTPLQ 273
Cdd:PRK10572 201 DIESVAQHVCLSPSRLAHLFRQQLGISVLRWREDQRISRAKLLLQTTRMPIATIGRNVGYDDQLYFSRVFKKCTGASPSE 280
|
....*
gi 654551502 274 YRRRI 278
Cdd:PRK10572 281 FRARC 285
|
|
| PRK13503 |
PRK13503 |
HTH-type transcriptional activator RhaS; |
131-275 |
9.84e-13 |
|
HTH-type transcriptional activator RhaS;
Pssm-ID: 184094 [Multi-domain] Cd Length: 278 Bit Score: 66.62 E-value: 9.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654551502 131 IERILEQFQRLEGNEQTEA-CEVAFLVMQLMTFLPEQPQPYPPRQQTVASR-IMSWIEAHYASKFSLDQLAHDLGLSRSY 208
Cdd:PRK13503 124 VRQLVAQMEQQEESNDLEAiASREILFMQLLVLLRKSSLQENGENSDARLNqLLAWLEDHFAEEVNWEALADQFSLSLRT 203
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 654551502 209 TSRIFRQQTGGSIHEYLLTRRIKSSCDLLRYSDESIDTIALAVGFSEVTYFITCFKKMMRQTPLQYR 275
Cdd:PRK13503 204 LHRQLKQQTGLTPQRYLNRLRLLKARHLLRHSDASVTDIAYRCGFGDSNHFSTLFRREFSWSPRDIR 270
|
|
| PRK11511 |
PRK11511 |
MDR efflux pump AcrAB transcriptional activator MarA; |
181-284 |
4.26e-10 |
|
MDR efflux pump AcrAB transcriptional activator MarA;
Pssm-ID: 236920 [Multi-domain] Cd Length: 127 Bit Score: 56.65 E-value: 4.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654551502 181 IMSWIEAHYASKFSLDQLAHDLGLSRSYTSRIFRQQTGGSIHEYLLTRRIKSSCDLLRYSDESIDTIALAVGFSEVTYFI 260
Cdd:PRK11511 14 ILDWIEDNLESPLSLEKVSERSGYSKWHLQRMFKKETGHSLGQYIRSRKMTEIAQKLKESNEPILYLAERYGFESQQTLT 93
|
90 100
....*....|....*....|....
gi 654551502 261 TCFKKMMRQTPLQYRrrilSTRMP 284
Cdd:PRK11511 94 RTFKNYFDVPPHKYR----MTNMQ 113
|
|
| PRK13500 |
PRK13500 |
HTH-type transcriptional activator RhaR; |
13-275 |
4.84e-10 |
|
HTH-type transcriptional activator RhaR;
Pssm-ID: 184091 [Multi-domain] Cd Length: 312 Bit Score: 59.35 E-value: 4.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654551502 13 DRQAISFNRLYASSAIYYHWHQCVELLYISSGYGIVVVDNQHYTARPGRLFIfppfrlhkvqVDHSDKNPYHRTTMHIEQ 92
Cdd:PRK13500 46 DQQAVAVADRYPQDVFAEHTHDFCELVIVWRGNGLHVLNDRPYRITRGDLFY----------IHADDKHSYASVNDLVLQ 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654551502 93 AVV--ESALSAFPRHQARFAALAASNLPAQIYDLSEHAAFIERILEQFQRLEGNE---QTEACEVAF--LVMQLMTFLPE 165
Cdd:PRK13500 116 NIIycPERLKLNLDWQGAIPGFSASAGQPHWRLGSVGMAQARQVIGQLEHESSQHvpfANEMAELLFgqLVMLLNRHRYT 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654551502 166 QPQPYPPRQQTVASRIMSWIEAHYASKFSLDQLAHDLGLSRSYTSRIFRQQTGGSIHEYLLTRRIKSSCDLLRYSDESID 245
Cdd:PRK13500 196 SDSLPPTSSETLLDKLITRLAASLKSPFALDKFCDEASCSERVLRQQFRQQTGMTINQYLRQVRVCHAQYLLQHSRLLIS 275
|
250 260 270
....*....|....*....|....*....|
gi 654551502 246 TIALAVGFSEVTYFITCFKKMMRQTPLQYR 275
Cdd:PRK13500 276 DISTECGFEDSNYFSVVFTRETGMTPSQWR 305
|
|
| PRK09685 |
PRK09685 |
DNA-binding transcriptional activator FeaR; Provisional |
198-279 |
7.39e-10 |
|
DNA-binding transcriptional activator FeaR; Provisional
Pssm-ID: 236612 [Multi-domain] Cd Length: 302 Bit Score: 58.50 E-value: 7.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654551502 198 LAHDLGLSRSYTSRIFRQQtGGSIHEYLLTRRIKSSCDLLR--YSDESIDTIALAVGFSEVTYFITCFKKMMRQTPLQYR 275
Cdd:PRK09685 220 IAGELGISVRSLYRLFAEQ-GLVVAQYIRNRRLDRCADDLRpaADDEKITSIAYKWGFSDSSHFSTAFKQRFGVSPGEYR 298
|
....
gi 654551502 276 RRIL 279
Cdd:PRK09685 299 RKFR 302
|
|
| ftrA |
PRK09393 |
transcriptional activator FtrA; Provisional |
179-277 |
7.64e-10 |
|
transcriptional activator FtrA; Provisional
Pssm-ID: 181818 [Multi-domain] Cd Length: 322 Bit Score: 58.44 E-value: 7.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654551502 179 SRIMSWIEAHYASKFSLDQLAHDLGLSRSYTSRIFRQQTGGSIHEYLLTRRIKSSCDLLRYSDESIDTIALAVGFSEVTY 258
Cdd:PRK09393 221 GPLIDWMRAHLAEPHTVASLAARAAMSPRTFLRRFEAATGMTPAEWLLRERLARARDLLESSALSIDQIAERAGFGSEES 300
|
90
....*....|....*....
gi 654551502 259 FITCFKKMMRQTPLQYRRR 277
Cdd:PRK09393 301 LRHHFRRRAATSPAAYRKR 319
|
|
| PRK15121 |
PRK15121 |
MDR efflux pump AcrAB transcriptional activator RobA; |
181-276 |
7.93e-10 |
|
MDR efflux pump AcrAB transcriptional activator RobA;
Pssm-ID: 185076 [Multi-domain] Cd Length: 289 Bit Score: 58.48 E-value: 7.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654551502 181 IMSWIEAHYASKFSLDQLAHDLGLSRSYTSRIFRQQTGGSIHEYLLTRRIKSSCDLLRYSDESIDTIALAVGFSEVTYFI 260
Cdd:PRK15121 10 LLIWLEGHLDQPLSLDNVAAKAGYSKWHLQRMFKDVTGHAIGAYIRARRLSKAAVALRLTSRPILDIALQYRFDSQQTFT 89
|
90
....*....|....*.
gi 654551502 261 TCFKKMMRQTPLQYRR 276
Cdd:PRK15121 90 RAFKKQFAQTPALYRR 105
|
|
| PRK10371 |
PRK10371 |
transcriptional regulator MelR; |
179-276 |
9.69e-10 |
|
transcriptional regulator MelR;
Pssm-ID: 182416 [Multi-domain] Cd Length: 302 Bit Score: 58.29 E-value: 9.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654551502 179 SRIMSWIEAHYASKFSLDQLAHDLGLSRSYTSRIFRQQTGGSIHEYLLTRRIKSSCDLLRYSDESIDTIALAVGFSEVTY 258
Cdd:PRK10371 194 SQMLGFIAENYDQALTINDVAEHVKLNANYAMGIFQRVMQLTMKQYITAMRINHVRALLSDTDKSILDIALTAGFRSSSR 273
|
90
....*....|....*...
gi 654551502 259 FITCFKKMMRQTPLQYRR 276
Cdd:PRK10371 274 FYSTFGKYVGMSPQQYRK 291
|
|
| PRK13501 |
PRK13501 |
HTH-type transcriptional activator RhaR; |
181-277 |
1.32e-09 |
|
HTH-type transcriptional activator RhaR;
Pssm-ID: 184092 [Multi-domain] Cd Length: 290 Bit Score: 57.61 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654551502 181 IMSWIEAHYASKFSLDQLAHDLGLSRSYTSRIFRQQTGGSIHEYLLTRRIKSSCDLLRYSDESIDTIALAVGFSEVTYFI 260
Cdd:PRK13501 181 IMSALQQSLGAYFDMADFCHKNQLVERSLKQLFRQQTGMSISHYLRQIRLCHAKCLLRGSEHRISDIAARCGFEDSNYFS 260
|
90
....*....|....*..
gi 654551502 261 TCFKKMMRQTPLQYRRR 277
Cdd:PRK13501 261 AVFTREAGMTPRDYRQR 277
|
|
| PRK10219 |
PRK10219 |
superoxide response transcriptional regulator SoxS; |
181-278 |
5.53e-09 |
|
superoxide response transcriptional regulator SoxS;
Pssm-ID: 182314 [Multi-domain] Cd Length: 107 Bit Score: 53.01 E-value: 5.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654551502 181 IMSWIEAHYASKFSLDQLAHDLGLSRSYTSRIFRQQTGGSIHEYLLTRRIKSSCDLLRYSDESIDTIALAVGFSEVTYFI 260
Cdd:PRK10219 10 LIAWIDEHIDQPLNIDVVAKKSGYSKWYLQRMFRTVTHQTLGDYIRQRRLLLAAVELRTTERPIFDIAMDLGYVSQQTFS 89
|
90
....*....|....*...
gi 654551502 261 TCFKKMMRQTPLQYRRRI 278
Cdd:PRK10219 90 RVFRRQFDRTPSDYRHRL 107
|
|
| PRK13502 |
PRK13502 |
HTH-type transcriptional activator RhaR; |
13-275 |
1.42e-08 |
|
HTH-type transcriptional activator RhaR;
Pssm-ID: 184093 [Multi-domain] Cd Length: 282 Bit Score: 54.68 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654551502 13 DRQAISFNRLYASSAIYYHWHQCVELLYISSGYGIVVVDNQHYTARPGRLFIfppfrlhkvqVDHSDKNPYHRTTMHIEQ 92
Cdd:PRK13502 16 EQQAVTVADRYPQDVFAEHTHEFCELVMVWRGNGLHVLNERPYRITRGDLFY----------IRAEDKHSYTSVNDLVLQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654551502 93 AVV------------ESALSAFPRHQA----RFAALAAsNLPAQIYDLSEHAAfierileQFQRLEGNEQTEACeVAFLV 156
Cdd:PRK13502 86 NIIycperlklnvnwQAMIPGFQGAQWhphwRLGSMGM-NQARQVINQLEHES-------NGRDPLANEMAELL-FGQLV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654551502 157 MQLMTFLPEQPQPYPPRQQTVASRIMSWIEAHYASKFSLDQLAHDLGLSRSYTSRIFRQQTGGSIHEYLLTRRIKSSCDL 236
Cdd:PRK13502 157 MTLKRHRYATDDLPATSRETLLDKLITALANSLECPFALDAFCQQEQCSERVLRQQFRAQTGMTINQYLRQVRICHAQYL 236
|
250 260 270
....*....|....*....|....*....|....*....
gi 654551502 237 LRYSDESIDTIALAVGFSEVTYFITCFKKMMRQTPLQYR 275
Cdd:PRK13502 237 LQHSPLMISEISMQCGFEDSNYFSVVFTRETGMTPSQWR 275
|
|
| PRK15185 |
PRK15185 |
transcriptional regulator HilD; Provisional |
176-271 |
4.41e-08 |
|
transcriptional regulator HilD; Provisional
Pssm-ID: 185107 [Multi-domain] Cd Length: 309 Bit Score: 53.46 E-value: 4.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654551502 176 TVASRIMSWIEAHYASKFSLDQLAHDLGLSRSYTSRIFRQQtGGSIHEYLLTRRIKSSCDLLRYSDESIDTIALAVGFSE 255
Cdd:PRK15185 206 TLKERVYNIISSSPSRQWKLTDVADHIFMSTSTLKRKLAEE-GTSFSDIYLSARMNQAAKLLRIGNHNVNAVALKCGYDS 284
|
90
....*....|....*.
gi 654551502 256 VTYFITCFKKMMRQTP 271
Cdd:PRK15185 285 TSYFIQCFKKYFKTTP 300
|
|
| HTH_AraC |
pfam00165 |
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ... |
185-225 |
6.19e-08 |
|
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the N-terminal arm of AraC binds to the DNA binding domain (pfam00165) and helps to hold the two DNA binding domains in a relative orientation that favours DNA looping. In the presence of arabinose, the arms bind over the arabinose on the dimerization domain, thus freeing the DNA-binding domains. The freed DNA-binding domains are then able to assume a conformation suitable for binding to the adjacent DNA sites that are utilized when AraC activates transcription, and hence AraC ceases looping the DNA when arabinose is added.
Pssm-ID: 425497 [Multi-domain] Cd Length: 42 Bit Score: 47.92 E-value: 6.19e-08
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 654551502 185 IEAHYASKFSLDQLAHDLGLSRSYTSRIFRQQTGGSIHEYL 225
Cdd:pfam00165 1 LRENLSTNLTIADIADELGFSRSYFSRLFKKYTGVTPSQYR 41
|
|
| AraC_binding |
pfam02311 |
AraC-like ligand binding domain; This family represents the arabinose-binding and dimerization ... |
30-137 |
4.13e-07 |
|
AraC-like ligand binding domain; This family represents the arabinose-binding and dimerization domain of the bacterial gene regulatory protein AraC. The domain is found in conjunction with the helix-turn-helix (HTH) DNA-binding motif pfam00165. This domain is distantly related to the Cupin domain pfam00190.
Pssm-ID: 396749 [Multi-domain] Cd Length: 134 Bit Score: 48.20 E-value: 4.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654551502 30 YHWHQCVELLYISSGYGIVVVDNQHYTARPGRLFIFPPFRLHKVQVDHSDknPYHRTTMHIEQAVVESALSAFPRHQARF 109
Cdd:pfam02311 18 PHVHDFYVIGYIERGVGRFRLNGRTYHLGPGDLFLLPPGEPHDYEPESED--GWRYRWLYFEPELLERILADISILAGGP 95
|
90 100 110
....*....|....*....|....*....|..
gi 654551502 110 AAL----AASNLPAQIYDLSEHAAFIERILEQ 137
Cdd:pfam02311 96 LPLlrdpELAALLRALFRLLEEAGRSDDLLAE 127
|
|
| QdoI |
COG1917 |
Cupin domain protein related to quercetin dioxygenase [General function prediction only]; |
31-80 |
1.04e-06 |
|
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
Pssm-ID: 441521 [Multi-domain] Cd Length: 99 Bit Score: 46.38 E-value: 1.04e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 654551502 31 HWHQCVELLYISSGYGIVVVDNQHYTARPGRLFIFPPFRLHKVQVDHSDK 80
Cdd:COG1917 39 HSHPGEELIYVLEGEGEVEVGGEEYELKPGDVVFIPPGVPHAFRNLGDEP 88
|
|
| PRK09978 |
PRK09978 |
DNA-binding transcriptional regulator GadX; Provisional |
177-277 |
2.15e-06 |
|
DNA-binding transcriptional regulator GadX; Provisional
Pssm-ID: 137624 [Multi-domain] Cd Length: 274 Bit Score: 48.00 E-value: 2.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654551502 177 VASRIMSWIEAHYASKFSLDQLAHDLGLSRSYTSRIFRQQtgGSIHEYLLTR-RIKSSCDLLRYSDESIDTIALAVGFSE 255
Cdd:PRK09978 143 MRTRVCTVINNNIAHEWTLARIASELLMSPSLLKKKLREE--ETSYSQLLTEcRMQRALQLIVIHGFSIKRVAVSCGYHS 220
|
90 100
....*....|....*....|..
gi 654551502 256 VTYFITCFKKMMRQTPLQYRRR 277
Cdd:PRK09978 221 VSYFIYVFRNYYGMTPTEYQER 242
|
|
| PRK15186 |
PRK15186 |
AraC family transcriptional regulator; Provisional |
176-282 |
2.51e-06 |
|
AraC family transcriptional regulator; Provisional
Pssm-ID: 185108 [Multi-domain] Cd Length: 291 Bit Score: 47.75 E-value: 2.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654551502 176 TVASRIMSWIEAHYASKFSLDQLAHDLGLSRSYTSRIFRQQTGgSIHEYLLTRRIKSSCDLLRYSDESIDTIALAVGFSE 255
Cdd:PRK15186 181 TLAENIYNIIISDISRKWALKDISDSLYMSCSTLKRKLKQENT-SFSEVYLNARMNKATKLLRNSEYNITRVAYMCGYDS 259
|
90 100
....*....|....*....|....*..
gi 654551502 256 VTYFITCFKKMMRQTPLQYRRRILSTR 282
Cdd:PRK15186 260 ASYFTCVFKKHFKTTPSEFLAFLSSSR 286
|
|
| cupin_MmsR-like_N |
cd06986 |
AraC/XylS family transcriptional regulators similar to MmsR, N-terminal cupin domain; This ... |
38-79 |
2.81e-05 |
|
AraC/XylS family transcriptional regulators similar to MmsR, N-terminal cupin domain; This family contains bacterial proteins containing an AraC/XylS family helix-turn-helix (HTH) DNA-binding domain C-terminal to a cupin domain, and may be possible transcriptional regulators. Included is MmsR, a bacterial transcriptional regulator thought to positively regulate the expression of the mmsAB operon. The mmsAB operon contains two structural genes involved in valine metabolism: mmsA which encodes methylmalonate-semialdehyde dehydrogenase, and mmsB which encodes 3-hydroxyisobutyrate dehydrogenase. The cupin domain of members of this subfamily does not contain a metal binding site.
Pssm-ID: 380391 [Multi-domain] Cd Length: 84 Bit Score: 41.70 E-value: 2.81e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 654551502 38 LLYISSGYGIVVVDNQHYTARPGRLFIFPPFRLHKVQVDHSD 79
Cdd:cd06986 31 LHYVLSGKGTFSVNGKTYHLKAGQGFLIPPGEPHSYGADEDD 72
|
|
| Cupin_2 |
pfam07883 |
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ... |
31-73 |
8.06e-05 |
|
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' is the Latin term for a small barrel).
Pssm-ID: 462300 [Multi-domain] Cd Length: 71 Bit Score: 39.93 E-value: 8.06e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 654551502 31 HWH-QCVELLYISSGYGIVVVDNQHYTARPGRLFIFPPFRLHKV 73
Cdd:pfam07883 14 HRHpGEDEFFYVLEGEGELTVDGEEVVLKAGDSVYFPAGVPHRF 57
|
|
| PRK10296 |
PRK10296 |
DNA-binding transcriptional regulator ChbR; Provisional |
177-282 |
6.66e-04 |
|
DNA-binding transcriptional regulator ChbR; Provisional
Pssm-ID: 182362 [Multi-domain] Cd Length: 278 Bit Score: 40.51 E-value: 6.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654551502 177 VASRIMSWIEA-----HYASKFSLDQLAHDLGLS---RSY----TSRIFRQQTGGSIHEYlltrRIKSSCDLLRYSDESI 244
Cdd:PRK10296 165 VIDDIPQWLKAtvekmHDKEQFSESALENMVRLSgksQEYltraTRRYYGKTPMQIINEI----RINFAKKQLEMTNYSV 240
|
90 100 110
....*....|....*....|....*....|....*...
gi 654551502 245 DTIALAVGFSEVTYFITCFKKMMRQTPLQYRRRILSTR 282
Cdd:PRK10296 241 TDIAFEAGYSSPSLFIKTFKKLTSFTPGSYRKKLTEFN 278
|
|
| HTH_AraC |
pfam00165 |
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ... |
240-276 |
8.55e-04 |
|
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the N-terminal arm of AraC binds to the DNA binding domain (pfam00165) and helps to hold the two DNA binding domains in a relative orientation that favours DNA looping. In the presence of arabinose, the arms bind over the arabinose on the dimerization domain, thus freeing the DNA-binding domains. The freed DNA-binding domains are then able to assume a conformation suitable for binding to the adjacent DNA sites that are utilized when AraC activates transcription, and hence AraC ceases looping the DNA when arabinose is added.
Pssm-ID: 425497 [Multi-domain] Cd Length: 42 Bit Score: 36.36 E-value: 8.55e-04
10 20 30
....*....|....*....|....*....|....*..
gi 654551502 240 SDESIDTIALAVGFSEvTYFITCFKKMMRQTPLQYRR 276
Cdd:pfam00165 7 TNLTIADIADELGFSR-SYFSRLFKKYTGVTPSQYRH 42
|
|
| COG3837 |
COG3837 |
Uncharacterized conserved protein, cupin superfamily [Function unknown]; |
5-71 |
1.31e-03 |
|
Uncharacterized conserved protein, cupin superfamily [Function unknown];
Pssm-ID: 443048 [Multi-domain] Cd Length: 115 Bit Score: 37.69 E-value: 1.31e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 654551502 5 QLLERITLDRQAISFNRLYA-SSAIYYHWHQCV-ELLYISSGYGIVVVDNQHYTARPGRLFIFPPFRLH 71
Cdd:COG3837 18 RLGDALGLTRLGVNLITLPPgASSSPYHAHSAEeEFVYVLEGELTLRIGGEEYVLEPGDSVGFPAGVPH 86
|
|
| PRK15044 |
PRK15044 |
transcriptional regulator SirC; Provisional |
176-278 |
6.57e-03 |
|
transcriptional regulator SirC; Provisional
Pssm-ID: 185004 [Multi-domain] Cd Length: 295 Bit Score: 37.32 E-value: 6.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654551502 176 TVASRIMSWIEAHYASKFSLDQLAHDLGLSRSYTSRIFRQQTGgSIHEYLLTRRIKSSCDLLRYSDESIDTIALAVGFSE 255
Cdd:PRK15044 192 TTKEKVYNIIISDLTRKWSQAEVAGKLFMSVSSLKRKLAAEEV-SFSKIYLDARMNQAIKLLRMGAGNISQVATMCGYDT 270
|
90 100
....*....|....*....|...
gi 654551502 256 VTYFITCFKKMMRQTPLQYRRRI 278
Cdd:PRK15044 271 PSYFIAIFKRHFKITPLSFMRTM 293
|
|
| cupin_MAE_RS03005 |
cd06987 |
Microcystis aeruginosa MAE_RS03005 and related proteins, cupin domain; This family includes ... |
33-88 |
8.40e-03 |
|
Microcystis aeruginosa MAE_RS03005 and related proteins, cupin domain; This family includes bacterial and some eukaryotic proteins homologous to MAE_RS03005, a Microcystis aeruginosa protein of unknown function. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.
Pssm-ID: 380392 [Multi-domain] Cd Length: 122 Bit Score: 35.70 E-value: 8.40e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 654551502 33 HQCVELLYISSGYGIVVVDNQHYTARPGRLFIFPPFRLHKVQVDHSDKnPYHRTTM 88
Cdd:cd06987 47 PAAHEMFFVLAGEGRAYCDGQRVPLRPGDALVVPPGSEHVIENTGSGR-LYCLTLM 101
|
|
| cupin_RmlC-like |
cd02208 |
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ... |
17-74 |
8.67e-03 |
|
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP (deoxythymidine diphosphates)-4-dehydrorhamnose 3,5-epimerase)-like cupins. RmlC is a dTDP-sugar isomerase involved in the synthesis of L-rhamnose, a saccharide required for the virulence of some pathogenic bacteria. Cupins are a functionally diverse superfamily originally discovered based on the highly conserved motif found in germin and germin-like proteins. This conserved motif forms a beta-barrel fold found in all of the cupins, giving rise to the name cupin ('cupa' is the Latin term for small barrel). The active site of members of this superfamily is generally located at the center of a conserved barrel and usually includes a metal ion. The different functional classes in this superfamily include single domain bacterial isomerases and epimerases involved in the modification of cell wall carbohydrates, two domain bicupins such as the desiccation-tolerant seed storage globulins, and multidomain nuclear transcription factors involved in legume root nodulation.
Pssm-ID: 380338 [Multi-domain] Cd Length: 73 Bit Score: 34.38 E-value: 8.67e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 654551502 17 ISFNRLYASSAIYYHWHQ-CVELLYISSGYGIVVVDNQ-HYTARPGRLFIFPPFRLHKVQ 74
Cdd:cd02208 1 ISVVTLPPGTSSPPHWHPeQDEIFYVLSGEGELTLDDGeTVELKAGDIVLIPPGVPHSFV 60
|
|
| cupin_DddK |
cd06988 |
Dimethylsulfoniopropionate lyase DddK and related proteins, cupin domain; This family includes ... |
31-74 |
9.21e-03 |
|
Dimethylsulfoniopropionate lyase DddK and related proteins, cupin domain; This family includes mostly bacterial proteins homologous to dimethylsulfoniopropionate lyase DddK from marine bacterium Pelagibacter. DddK cleaves dimethylsulfoniopropionate (DMSP), the organic osmolyte and antioxidant produced in marine environments, and yields acrylate and the climate-active gas dimethyl sulfide (DMS). DddK contains a double-stranded beta-helical motif which utilizes various divalent metal ions as cofactors for catalytic activity; however, nickel, an abundant metal ion in marine environments, confers the highest DMSP lyase activity. Also included in this family is Plu4264, a Photorhabdus luminescens manganese-containing cupin shown to have similar metal binding site to TM1287 decarboxylase, but two very different substrate binding pockets. The Plu4264 binding pocket shows a cavity and substrate entry point more than twice as large as and more hydrophobic than TM1287, suggesting that Plu4264 accepts a substrate that is significantly larger than that of TM1287, a putative oxalate decarboxylase. Thus, the function of Plu4264 could be similar to that of TM1287 but with a larger, less charged substrate. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.
Pssm-ID: 380393 [Multi-domain] Cd Length: 76 Bit Score: 34.52 E-value: 9.21e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 654551502 31 HWHQCVELLYISSGYGIVVVDNQHYTARPGRLFIFPPFRLHKVQ 74
Cdd:cd06988 18 HSHHEYEIFIVISGKGIVVVDGEREPVKAGDVVYIPPGTEHYVK 61
|
|
| |
